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J Biol Chem, Vol. 273, Issue 15, 8849-8859, April 10, 1998
The Assembly System for the Lipopolysaccharide R2 Core-type of
Escherichia coli Is a Hybrid of Those Found in
Escherichia coli K-12 and Salmonella
enterica
STRUCTURE AND FUNCTION OF THE R2 WaaK AND WaaL
HOMOLOGS
David E.
Heinrichs ,
Mario A.
Monteiro¶,
Malcolm B.
Perry¶, and
Chris
Whitfield
From the Department of Microbiology, University of
Guelph, Guelph, Ontario, Canada N1G 2W1 and ¶ Institute
for Biological Sciences, National Research Council,
Ottawa, Ontario, Canada K1A OR6
In Escherichia coli F632, the
14-kilobase pair chromosomal region located between waaC
(formerly rfaC) and waaA (kdtA)
contains genes encoding enzymes required for the synthesis of the type R2 core oligosaccharide portion of lipopolysaccharide. Ten of the 13 open reading frames encode predicted products sharing greater than 90%
total similarity with homologs in E. coli K-12. However, the products of waaK (rfaK) and
waaL (rfaL) each resemble homologs in
Salmonella enterica serovar Typhimurium but
share little similarity with E. coli K-12. The F632 WaaK
and WaaL proteins therefore define differences between the type R2 and
K-12 outer core oligosaccharides of E. coli
lipopolysaccharides. Based on the chemical structure of the core
oligosaccharide of an E. coli F632
waaK::aacC1 mutant and in
vitro glycosyltransferase analyses, waaK encodes
UDP-N-acetylglucosamine:(glucose) lipopolysaccharide
1,2-N-acetylglucosaminyltransferase. The WaaK enzyme
adds a terminal GlcNAc side branch substituent that is crucial for the
recognition of core oligosaccharide acceptor by the O-polysaccharide
ligase, WaaL. Results of complementation analyses of E. coli K-12 and F632 waaL mutants suggest that
structural differences between the WaaL proteins play a role in
recognition of, and interaction with, terminal lipopolysaccharide core
moieties.
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.

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Copyright © 1998 by the American Society for Biochemistry and Molecular Biology.
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